{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Eaton AF"],"funding":["NIDDK NIH HHS","Inflammatory Bowel Disease Center","National Institutes of Health","Boston Area Diabetes and Endocrinology Research Center","NIH HHS"],"pagination":["zqae025"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11237898"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(4)"],"pubmed_abstract":["The proton pumping V-ATPase drives essential biological processes, such as acidification of intracellular organelles. Critically, the V-ATPase domains, V1 and VO, must assemble to produce a functional holoenzyme. V-ATPase dysfunction results in cancer, neurodegeneration, and diabetes, as well as systemic acidosis caused by reduced activity of proton-secreting kidney intercalated cells (ICs). However, little is known about the molecular regulation of V-ATPase in mammals. We identified a novel interactor of the mammalian V-ATPase, Drosophila melanogaster X chromosomal gene-like 1 (Dmxl1), aka Rabconnectin-3A. The yeast homologue of Dmxl1, Rav1p, is part of a complex that catalyzes the reversible assembly of the domains. We, therefore,hypothesized that Dmxl1 is a mammalian V-ATPase assembly f"],"journal":["Function (Oxford, England)"],"pubmed_title":["Dmxl1 Is an Essential Mammalian Gene that Is Required for V-ATPase Assembly and Function In Vivo."],"pmcid":["PMC11237898"],"funding_grant_id":["DK043351","T32 DK007540","P30 DK135043","DK135043","P30 DK043351","R01 DK121848","S10 OD021577","OD021577"],"pubmed_authors":["Eaton AF","Danielson EC","Merkulova M","Brown D","Capen D"],"additional_accession":[]},"is_claimable":false,"name":"Dmxl1 Is an Essential Mammalian Gene that Is Required for V-ATPase Assembly and Function In Vivo.","description":"The proton pumping V-ATPase drives essential biological processes, such as acidification of intracellular organelles. Critically, the V-ATPase domains, V1 and VO, must assemble to produce a functional holoenzyme. V-ATPase dysfunction results in cancer, neurodegeneration, and diabetes, as well as systemic acidosis caused by reduced activity of proton-secreting kidney intercalated cells (ICs). However, little is known about the molecular regulation of V-ATPase in mammals. We identified a novel interactor of the mammalian V-ATPase, Drosophila melanogaster X chromosomal gene-like 1 (Dmxl1), aka Rabconnectin-3A. The yeast homologue of Dmxl1, Rav1p, is part of a complex that catalyzes the reversible assembly of the domains. We, therefore,hypothesized that Dmxl1 is a mammalian V-ATPase assembly f","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2025-04-19T01:04:14.044Z","creation":"2025-04-07T12:00:54.165Z"},"accession":"S-EPMC11237898","cross_references":{"pubmed":["38984989"],"doi":["10.1093/function/zqae025"]}}